The proteins of axons prepared from myelinated axons and isolated as myelin-free entities were separated by sodium dodecyl sulfate polyacrylamide electrophoresis and found to consist of more than 10 different molecular weight species. The molecular weights range from 13 000 to over 200 000 with a prominent protein of molecular weight 47 000. The amino acid composition of the seven major proteins showed that the protein with a molecular weigt of 47 000 is distinct from all the other proteins analyzed. A group of three low molecular weight proteins have amino acid compositions which are similar to each other as do a group of three high molecular weight proteins although the two groups are distinctly different from each other and the major axonal protein. Histones, DNA, myelin basic protein and glycoprotein were absent from the proteins but neurotubule protein was present as indicated by cochicine binding activity in the axonal preparations. The cellular origin of these proteins and their relationship to other central nervous system proteins are discussed.